Zobrazeno 1 - 10
of 12
pro vyhledávání: '"U K, Schubart"'
Publikováno v:
The Journal of biological chemistry. 267(5)
p19 is a highly conserved 19-kDa cytosolic protein that undergoes phosphorylation in mammalian cells upon activation of several distinct signal transduction pathways. Its expression is widespread but developmentally regulated. To determine the in viv
Publikováno v:
Reproduction, fertility, and development. 4(2)
The p19/SCG10 gene family encodes two structurally related cellular proteins that are implicated in signal transduction during differentiation of mammalian cells. Previous evidence suggests that both genes are expressed in a stage-specific manner but
Publikováno v:
Journal of Biological Chemistry. 262:11871-11877
We report the purification from bovine brain and describe some of the properties of a 19-kDa protein, p19, which we have previously shown to undergo hormone-dependent, cAMP-mediated phosphorylation in several peptide hormone-producing tumor cells. Th
Autor:
U K Schubart, K L Fields
Publikováno v:
The Journal of Cell Biology
This report describes the cytoskeleton nature of a 60,000-mol-wt protein, P60, previously shown to undergo Ca2+ influx-induced phosphorylation concomitant with insulin release in hamster insulinoma cells. Four lines of evidence suggest that P60 is an
Autor:
U K Schubart
Publikováno v:
Journal of Biological Chemistry. 257:12231-12238
Publikováno v:
The Journal of biological chemistry. 262(24)
We report the purification from bovine brain and describe some of the properties of a 19-kDa protein, p19, which we have previously shown to undergo hormone-dependent, cAMP-mediated phosphorylation in several peptide hormone-producing tumor cells. Th
Publikováno v:
The Journal of biological chemistry. 255(9)
Autor:
U K, Schubart
Publikováno v:
The Journal of biological chemistry. 257(20)
Publikováno v:
Federation proceedings. 41(7)
Both Ca2+ and cyclic AMP (cAMP) are implicated in the regulation of insulin release in the pancreatic beta cell. In hamster insulinoma cells used in our laboratory to study the mechanism of insulin release, Ca2+ and cAMP trigger secretion independent
Publikováno v:
The Journal of biological chemistry. 255(23)
Ca2+-dependent protein phosphorylation was studied in intact hamster insulinoma cells. Depolarizing concentrations of potassium which stimulate Ca2+ uptake and insulin release by these cells also increased phosphorylation of one peptide, Mr = 60,000